Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9KGN8 (IMDH_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inosine-5'-monophosphate dehydrogenase

Short name=IMP dehydrogenase
Short name=IMPD
Short name=IMPDH
EC=1.1.1.205
Gene names
Name:guaB
Ordered Locus Names:BH0020
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth By similarity. HAMAP-Rule MF_01964

Catalytic activity

Inosine 5'-phosphate + NAD+ + H2O = xanthosine 5'-phosphate + NADH. HAMAP-Rule MF_01964

Cofactor

Potassium By similarity. HAMAP-Rule MF_01964

Enzyme regulation

Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH By similarity. HAMAP-Rule MF_01964

Pathway

Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1. HAMAP-Rule MF_01964

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01964

Sequence similarities

Belongs to the IMPDH/GMPR family.

Contains 2 CBS domains.

Ontologies

Keywords
   Biological processGMP biosynthesis
Purine biosynthesis
   DomainCBS domain
Repeat
   LigandMetal-binding
NAD
Potassium
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processGMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Molecular_functionIMP dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

adenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 485485Inosine-5'-monophosphate dehydrogenase HAMAP-Rule MF_01964
PRO_0000093690

Regions

Domain95 – 15460CBS 1
Domain155 – 21561CBS 2
Nucleotide binding299 – 3013NAD By similarity
Region339 – 3413IMP binding By similarity
Region362 – 3632IMP binding By similarity
Region386 – 3905IMP binding By similarity

Sites

Active site3061Thioimidate intermediate By similarity
Metal binding3011Potassium; via carbonyl oxygen By similarity
Metal binding3031Potassium; via carbonyl oxygen By similarity
Metal binding3061Potassium; via carbonyl oxygen By similarity
Metal binding4681Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4691Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Metal binding4701Potassium; via carbonyl oxygen; shared with tetrameric partner By similarity
Binding site2491NAD By similarity
Binding site3041IMP By similarity
Binding site4141IMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KGN8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: D0B64489E5CF8B60

FASTA48552,429
        10         20         30         40         50         60 
MWENKFQKEG LTFDDVLLVP AKSEVLPRDV SVKTKLTETL QLNIPIISAG MDTVTEAKMA 

        70         80         90        100        110        120 
IAIAREGGLG IIHKNMSVEE QAEQVDRVKR SESGVITNPF FLTPDRQVFD AEHLMGKYRI 

       130        140        150        160        170        180 
SGVPIVDEDQ KLVGILTNRD LRFIEDYSTL IDDVMTKENL VTAPVGTTLK EAEEILQKHK 

       190        200        210        220        230        240 
IEKLPLVDES GTLKGLITIK DIEKVIEFPN SAKDSQGRLI VGAAVGVSAD TDVRVAALVE 

       250        260        270        280        290        300 
AGVDVIVIDT AHGHSKGVLE KVKAIREQYP DLTIIAGNVA TAEATRDLIE AGANVVKVGI 

       310        320        330        340        350        360 
GPGSICTTRI VAGIGVPQIT AVYDCANEAR KHGVPIIADG GIKYSGDIVK ALAAGGHAVM 

       370        380        390        400        410        420 
LGSLLAGVSE SPGEREIFQG RQFKVYRGMG SLGAMEKGSK DRYFQENNQK LVPEGIEGRI 

       430        440        450        460        470        480 
PYKGPLHDTI HQLVGGIRAG MGYCGTKTID ELRENTQFIR ITGAGLRESH PHDVQITKEA 


PNYTL 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB03739.1.
PIRD83652.
RefSeqNP_240886.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KGN8.
SMRQ9KGN8. Positions 2-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH0020.

Proteomic databases

PRIDEQ9KGN8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB03739; BAB03739; BAB03739.
GeneID890466.
KEGGbha:BH0020.
PATRIC18936854. VBIBacHal18977_0021.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0517.
KOK00088.
OMAHGHSKNI.
OrthoDBEOG6GTZPV.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-23-MONOMER.
UniPathwayUPA00601; UER00295.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01964. IMPDH.
InterProIPR013785. Aldolase_TIM.
IPR000644. CBS_dom.
IPR005990. IMP_DH.
IPR015875. IMP_DH/GMP_Rdtase_CS.
IPR001093. IMP_DH_GMPRt.
[Graphical view]
PfamPF00571. CBS. 2 hits.
PF00478. IMPDH. 1 hit.
[Graphical view]
PIRSFPIRSF000130. IMPDH. 1 hit.
SMARTSM00116. CBS. 2 hits.
[Graphical view]
TIGRFAMsTIGR01302. IMP_dehydrog. 1 hit.
PROSITEPS51371. CBS. 2 hits.
PS00487. IMP_DH_GMP_RED. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIMDH_BACHD
AccessionPrimary (citable) accession number: Q9KGN8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways